scholarly journals Clinical course of patients with Fabry disease who were switched from agalsidase-β to agalsidase-α

2014 ◽  
Vol 16 (10) ◽  
pp. 766-772 ◽  
Author(s):  
Kazuya Tsuboi ◽  
Hiroshi Yamamoto
Keyword(s):  
Fabry Disease ◽  
Clinical Course ◽  
Agalsidase Α ◽  
Agalsidase Β

scholarly journals Generation and Characterization of a Polyclonal Human Reference Antibody to Measure Anti-Drug Antibody Titers in Patients with Fabry Disease

2021 ◽  
Vol 22 (5) ◽  
pp. 2680
Author(s):  
Malte Lenders ◽  
David Scharnetzki ◽  
Ali Heidari ◽  
Daniele Di Iorio ◽  
Seraphine Valeska Wegner ◽  
...  
Keyword(s):  
Fabry Disease ◽  
Serum Samples ◽  
Enzyme Replacement ◽  
Patients At Risk ◽  
Antibody Titers ◽  
Male Patients ◽  
The Individual ◽  
Agalsidase Α ◽  
Agalsidase Β

Male patients with Fabry disease (FD) are at high risk for the formation of antibodies to recombinant α-galactosidase A (AGAL), used for enzyme replacement therapy. Due to the rapid disease progression, the identification of patients at risk is highly warranted. However, currently suitable references and standardized protocols for anti-drug antibodies (ADA) determination do not exist. Here we generate a comprehensive patient-derived antibody mixture as a reference, allowing ELISA-based quantification of antibody titers from individual blood samples. Serum samples of 22 male patients with FD and ADAs against AGAL were pooled and purified by immune adsorption. ADA-affinities against agalsidase-α, agalsidase-β and Moss-AGAL were measured by quartz crystal microbalance with dissipation monitoring (QCM-D). AGAL-specific immune adsorption generated a polyclonal ADA mixture showing a concentration-dependent binding and inhibition of AGAL. Titers in raw sera and from purified total IgGs (r2 = 0.9063 and r2 = 0.8952, both p < 0.0001) correlated with the individual inhibitory capacities of ADAs. QCM-D measurements demonstrated comparable affinities of the reference antibody for agalsidase-α, agalsidase-β and Moss-AGAL (KD: 1.94 ± 0.11 µM, 2.46 ± 0.21 µM, and 1.33 ± 0.09 µM, respectively). The reference antibody allows the ELISA-based ADA titer determination and quantification of absolute concentrations. Furthermore, ADAs from patients with FD have comparable affinities to agalsidase-α, agalsidase-β and Moss-AGAL.

Differences between agalsidase α and agalsidase β in the treatment of Fabry disease

2017 ◽  
Vol 149 (6) ◽  
pp. 270
Author(s):  
Jordi Pérez-López ◽  
Alfonso Domínguez Gil-Hurlé ◽  
Mónica López Rodríguez
Keyword(s):  
Fabry Disease ◽  
Agalsidase Α ◽  
Agalsidase Β

scholarly journals Effects of agalsidase-β administration on vascular function and blood pressure in familial Anderson–Fabry disease

2020 ◽  
Author(s):  
Cosimo Andrea Stamerra ◽  
Martina De Feo ◽  
Vanessa Castelli ◽  
Michele d’Angelo ◽  
Annamaria Cimini ◽  
...  
Keyword(s):  
Blood Pressure ◽  
Fabry Disease ◽  
Vascular Function ◽  
Agalsidase Β

scholarly journals Biomarkers in Anderson–Fabry Disease

2020 ◽  
Vol 21 (21) ◽  
pp. 8080
Author(s):  
Irene Simonetta ◽  
Antonino Tuttolomondo ◽  
Mario Daidone ◽  
Antonio Pinto
Keyword(s):  
Fabry Disease ◽  
Lysosomal Storage Disorder ◽  
Screening Tool ◽  
Clinical Course ◽  
Response To Treatment ◽  
Current Evidence ◽  
Diagnostic Process ◽  
Plasma Proteome ◽  
Lysosomal Storage ◽  
Clinical Progression

Fabry disease is a rare lysosomal storage disorder caused by a deficiency of α-galactosidase A, resulting in multisystemic involvement. Lyso-Gb3 (globotriaosylsphingosine), the deacylated form of Gb3, is currently measured in plasma as a biomarker of classic Fabry disease. Intensive research of biomarkers has been conducted over the years, in order to detect novel markers that may potentially be used in clinical practice as a screening tool, in the context of the diagnostic process and as an indicator of response to treatment. An interesting field of application of such biomarkers is the management of female heterozygotes who present difficulty in predictable clinical progression. This review aims to summarise the current evidence and knowledge about general and specific markers that are actually measured in subjects with confirmed or suspected Fabry disease; moreover, we report potential novel markers such as microRNAs. Recent proteomic or metabolomic studies are in progress bringing out plasma proteome profiles in Fabry patients: this assessment may be useful to characterize molecular pathology of the disease, to improve diagnostic process, and to monitor response to treatment. The management of Fabry disease may be improved by the identification of biomarkers that reflect clinical course, severity, and the progression of the disease.

Agalsidase-α/agalsidase-β

2010 ◽  
Vol &NA; (1286) ◽  
pp. 8
Author(s):  
&NA;
Keyword(s):  
Agalsidase Α ◽  
Agalsidase Β

scholarly journals Characterization of small fiber pathology in a mouse model of Fabry disease

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Lukas Hofmann ◽  
Dorothea Hose ◽  
Anne Grießhammer ◽  
Robert Blum ◽  
Frank Döring ◽  
...  
Keyword(s):  
Fabry Disease ◽  
Lysosomal Storage ◽  
Drg Neurons ◽  
Small Fiber ◽  
Pain Models ◽  
Life Threatening ◽  
Agalsidase Α ◽  
Deficient Mice

Fabry disease (FD) is a life-threatening X-linked lysosomal storage disorder caused by α-galactosidase A (α-GAL) deficiency. Small fiber pathology and pain are major FD symptoms of unknown pathophysiology. α-GAL deficient mice (GLA KO) age-dependently accumulate globotriaosylceramide (Gb3) in dorsal root ganglion (DRG) neurons paralleled by endoplasmic stress and apoptosis as contributors to skin denervation. Old GLA KO mice show increased TRPV1 protein in DRG neurons and heat hypersensitivity upon i.pl. capsaicin. In turn, GLA KO mice are protected from heat and mechanical hypersensitivity in neuropathic and inflammatory pain models based on reduced neuronal Ih and Nav1.7 currents. We show that in vitro α-GAL silencing increases intracellular Gb3 accumulation paralleled by loss of Nav1.7 currents, which is reversed by incubation with agalsidase-α and lucerastat. We provide first evidence of a direct Gb3 effect on neuronal integrity and ion channel function as potential mechanism underlying pain and small fiber pathology in FD.

scholarly journals Sustained, Long-Term Renal Stabilization After 54 Months of Agalsidase β Therapy in Patients with Fabry Disease

2007 ◽  
Vol 18 (5) ◽  
pp. 1547-1557 ◽  
Author(s):  
Dominique P. Germain ◽  
Stephen Waldek ◽  
Maryam Banikazemi ◽  
David A. Bushinsky ◽  
Joel Charrow ◽  
...  
Keyword(s):  
Fabry Disease ◽  
Agalsidase Β

scholarly journals Time to treatment benefit for adult patients with Fabry disease receiving agalsidase β: data from the Fabry Registry

2016 ◽  
Vol 53 (7) ◽  
pp. 495-502 ◽  
Author(s):  
Alberto Ortiz ◽  
Ademola Abiose ◽  
Daniel G Bichet ◽  
Gustavo Cabrera ◽  
Joel Charrow ◽  
...  
Keyword(s):  
Fabry Disease ◽  
Adult Patients ◽  
Treatment Benefit ◽  
Time To Treatment ◽  
Agalsidase Β
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